1ugo: Difference between revisions

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==Solution structure of the first Murine BAG domain of Bcl2-associated athanogene 5==
==Solution structure of the first Murine BAG domain of Bcl2-associated athanogene 5==
<StructureSection load='1ugo' size='340' side='right'caption='[[1ugo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1ugo' size='340' side='right'caption='[[1ugo]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ugo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UGO FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ugo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UGO FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FANTOM 2 cDNA 4930405J06 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ugo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ugo OCA], [https://pdbe.org/1ugo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ugo RCSB], [https://www.ebi.ac.uk/pdbsum/1ugo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ugo ProSAT], [https://www.topsan.org/Proteins/RSGI/1ugo TOPSAN]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ugo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ugo OCA], [https://pdbe.org/1ugo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ugo RCSB], [https://www.ebi.ac.uk/pdbsum/1ugo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ugo ProSAT], [https://www.topsan.org/Proteins/RSGI/1ugo TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/BAG5_MOUSE BAG5_MOUSE]] May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity).  
[https://www.uniprot.org/uniprot/BAG5_MOUSE BAG5_MOUSE] May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Aoki, M]]
[[Category: Aoki M]]
[[Category: Arakawa, T]]
[[Category: Arakawa T]]
[[Category: Carninci, P]]
[[Category: Carninci P]]
[[Category: Endoh, H]]
[[Category: Endoh H]]
[[Category: Hayashi, F]]
[[Category: Hayashi F]]
[[Category: Hayashizaki, Y]]
[[Category: Hayashizaki Y]]
[[Category: Hirota, H]]
[[Category: Hirota H]]
[[Category: Inoue, M]]
[[Category: Inoue M]]
[[Category: Kawai, J]]
[[Category: Kawai J]]
[[Category: Kigawa, T]]
[[Category: Kigawa T]]
[[Category: Matsuda, T]]
[[Category: Matsuda T]]
[[Category: Osanai, T]]
[[Category: Osanai T]]
[[Category: Structural genomic]]
[[Category: Seimiya K]]
[[Category: Seimiya, K]]
[[Category: Seki E]]
[[Category: Seki, E]]
[[Category: Shirouzu M]]
[[Category: Shirouzu, M]]
[[Category: Tanaka A]]
[[Category: Tanaka, A]]
[[Category: Terada T]]
[[Category: Terada, T]]
[[Category: Yabuki T]]
[[Category: Yabuki, T]]
[[Category: Yokoyama S]]
[[Category: Yokoyama, S]]
[[Category: Yoshida M]]
[[Category: Yoshida, M]]
[[Category: Chaperone]]
[[Category: Rsgi]]
[[Category: Triple helix bundle]]

Latest revision as of 02:53, 28 December 2023

Solution structure of the first Murine BAG domain of Bcl2-associated athanogene 5Solution structure of the first Murine BAG domain of Bcl2-associated athanogene 5

Structural highlights

1ugo is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

BAG5_MOUSE May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

ADP-ATP exchange by the molecular chaperone Hsp70 is enhanced by several cochaperones. BAG5 consists of five BAG domains and associates with the nucleotide-binding domain (NBD) of Hsp70. The overexpression of BAG5 in the cytosol reportedly disturbs Hsp70-mediated protein refolding and induces Parkinson's disease. In the present study, we found that the fifth BAG domain (BD5) of BAG5 is responsible for the interaction between Hsp70 and BAG5. We also determined the crystal structures of the BD5*NBD complex. BD5 binding caused two different types of NBD conformational changes, which both disrupted the nucleotide-binding groove. In fact, BD5 reduced the affinity of the NBD for ADP. Moreover, BD5, as well as the full-length BAG5, accelerated Hsp70-mediated refolding in an in vitro assay. Therefore, BAG5 can function as the nucleotide exchange factor of Hsp70 for the enhancement of protein refolding.

The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange.,Arakawa A, Handa N, Ohsawa N, Shida M, Kigawa T, Hayashi F, Shirouzu M, Yokoyama S Structure. 2010 Mar 10;18(3):309-19. PMID:20223214[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Arakawa A, Handa N, Ohsawa N, Shida M, Kigawa T, Hayashi F, Shirouzu M, Yokoyama S. The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange. Structure. 2010 Mar 10;18(3):309-19. PMID:20223214 doi:10.1016/j.str.2010.01.004
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